ID   D5ULF8_CELFN            Unreviewed;       587 AA.
AC   D5ULF8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=Cfla_1096 {ECO:0000313|EMBL:ADG74000.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS   18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG74000.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG74000.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC   NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688; DOI=10.4056/sigs.1012662;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001595};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|RuleBase:RU361134};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR   EMBL; CP001964; ADG74000.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5ULF8; -.
DR   STRING; 446466.Cfla_1096; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; cfl:Cfla_1096; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   Proteomes; UP000000849; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11334; AmyAc_TreS; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   NCBIfam; TIGR02456; treS_nterm; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000849}.
FT   DOMAIN          54..455
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          21..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  66645 MW;  C5CCF559746541D5 CRC64;
     MASPVATHRE PPPTTAAIAM TGLPERRQPD VPAPVATGGR DSNPDWYRTA VFYEVMLRTF
     ADSAGSGSGD LPGLIQRLDY LQWLGVDCLW LPPFHPSPLR DGGYDVSDYT AVAPQYGTLD
     DFRTLVTECH HRGMRIVVDL VMNHTSDQHP WFQASRSDPN GPYGDFYVWS DDNTRYQDAR
     IIFVDTETSN WTFDPVRRQY FWHRFFSHQP DLNFENPRVV DAMLDVARFW LHLGVDGFRL
     DAVPYLFEAE GTNCENLPET HQFLRKVRRM IDEEFPGRIM LAEANQWPED VVHYFGTEEE
     PECHMCFHFP VMPRIYYALR DQRATQIVDI LADTPPIPSS TGQWSTFLRN HDELTLEMVS
     TEERASMYGW YAPDSRMRAN VGIRRRLAPL LDNSRKEIEL AHALLLSLPG SPCLYYGDEI
     GMGDNIWLPD RDAVRTPMQW TPDRNAGFST ADPGKLYLPL VQSLVYHYGN VNVESQLAQP
     TSLLHWVHGM LAVRRQHPAL GLGTFEVVPC DNESVLTFLR RTDDETILVV ANMAATARAA
     TVTLPGWAGA ATRDVFGGAH FPDVRPDGTL TFTLGSREFY WLELTAS
//